Islet amyloid in type 2 (non-insulin-dependent) diabetes

APMIS. 1996 Jan;104(1):12-8. doi: 10.1111/j.1699-0463.1996.tb00680.x.


Amyloid deposits are found in pancreatic islets of 90% of type 2 (non-insulin-dependent) diabetic subjects at postmortem. Islet amyloid is formed from islet amyloid polypeptide (IAPP). IAPP is a 37 amino acid peptide which is a normal constituent of beta cells and is co-secreted with insulin in animals and in man. The causative factors for fibrillogenesis of IAPP are unclear, but could be related to the sequence of IAPP and abnormal production of the peptide. The lack of islet amyloid in rodent models of diabetes is due to proline substitutions in the amyloidogenic region of IAPP. Amyloid fibrils are deposited between beta cells and islet capillaries: fibrils in invaginations of the plasma membrane may interfere with membrane signalling and insulin release. Amyloid fibrils are formed within 2 days in culture in islets isolated from transgenic mice expressing the gene for human IAPP, but not in vivo. Overexpression and decreased clearance of human IAPP from islet spaces may be important factors. Progressive deposition of IAPP fibrils combined with the associated reduction in the insulin-secreting beta cells is likely to contribute to deterioration of islet function in the course of type 2 diabetes.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Amyloid / analysis*
  • Animals
  • Diabetes Mellitus, Type 2 / metabolism*
  • Diabetes Mellitus, Type 2 / pathology
  • Humans
  • Islets of Langerhans / metabolism*
  • Molecular Sequence Data


  • Amyloid